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J. Biol. Chem., Vol. 277, Issue 17, 14598-14611, April 26, 2002
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From the The lipooligosaccharide (LOS) of
Haemophilus influenzae contains sialylated glycoforms, and
a sialyltransferase, Lic3A, has been previously identified. We report
evidence for two additional sialyltransferases, SiaA, and LsgB, that
affect N-acetyllactosamine containing glycoforms. Mutations
in genes we have designated siaA and lsgB
affected only the sialylated glycoforms containing
N-acetylhexosamine. A mutation in siaA resulted
in the loss of glycoforms terminating in
sialyl-N-acetylhexosamine and the appearance of higher
molecular weight glycoforms, containing the addition of
phosphoethanolamine, N-acetylgalactosamine, and
N-acetylneuraminic acid. Chromosomal complementation of the
siaA mutant resulted in the expression of the original
sialylated LOS phenotype. A mutation in lic3A resulted in
the loss of sialylation only in glycoforms lacking N-acetylhexosamine and had no effect on sialylation of the
terminal N-acetyllactosamine epitope. A double mutant in
siaA and lic3A resulted in the complete loss of
sialylation of the terminal N-acetyllactosamine epitope and expression
of the higher molecular weight sialylated glycoforms seen in the
siaA mutant. Mutation of lsgB resulted in
persistence of sialylated glycoforms but a reduction in
N-acetyllactosamine containing glycoforms. A triple mutant
of siaA, lic3A, and lsgB contained
no sialylated glycoforms. These results demonstrate that the
sialylation of the LOS of H. influenzae is a complex process involving multiple sialyltransferases.
Haemophilus influenzae Type b Strain A2 Has Multiple
Sialyltransferases Involved in Lipooligosaccharide Sialylation*
§,
,,,,¶¶, and
Department of Microbiology, University of
Iowa, Iowa City, Iowa 52242, the Department of Pharmaceutical
Chemistry, University of California, San Francisco, California
94143-0446, the §§ Department of Biological
Sciences, Illinois State University, Normal, Illinois 61790, the
** Children's Research Institute and Departments of
Pediatrics, Ohio State University, Columbus, Ohio 43205, and the
¶¶ Buck Institute for Age Research,
Novato, California 94945
*
This work was supported by United States Public Health
Service NIAID, National Institutes of Health, Grants AI24616, AI65298 (to M. A. A.), and AI31254 (to B. W. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: United States Army Medical Research Institute
for Infectious Disease, Ft. Detrick, MD 21702-2152.
To whom correspondence and reprint requests should be
addressed: Dept. of Microbiology, University of Iowa, 51 Newton Rd., Iowa City, IA 52242. Tel.: 319-335-7807; Fax: 319-335-9006; E-mail: michael-apicella@uiowa.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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